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Investigating the Role of Helicobacter pylori PriA Protein
Author(s) -
Singh Aparna,
Blaskovic Dusan,
Joo Jungsoo,
Yang Zhen,
Jackson Sharon H.,
Coleman William G.,
Yan Ming
Publication year - 2016
Publication title -
helicobacter
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.206
H-Index - 79
eISSN - 1523-5378
pISSN - 1083-4389
DOI - 10.1111/hel.12283
Subject(s) - biology , helicobacter pylori , microbiology and biotechnology , mutant , dna repair , dna replication , in vivo , wild type , dna , gene , genetics
Abstract Background In bacteria, PriA protein, a conserved DEXH‐type DNA helicase, plays a central role in replication restart at stalled replication forks. Its unique DNA binding property allows it to recognize and stabilize stalled forks and the structures derived from them. PriA plays a very critical role in replication fork stabilization and DNA repair in E. coli and N. gonorrhoeae . In our in vivo expression technology screen, pri A gene was induced in vivo when Helicobacter pylori infects mouse stomach. Materials and Methods We decided to elucidate the role of H. pylori PriA protein in survival in mouse stomach, survival in gastric epithelial cells and macrophage cells, DNA repair, acid stress, and oxidative stress. Results The priA null mutant strain was unable to colonize mice stomach mucosa after long‐term infections. Mouse colonization was observed after 1 week of infection, but the levels were much lower than the wild‐type HpSS1 strain. PriA protein was found to be important for intracellular survival of epithelial cell‐/macrophage cell‐ingested H. pylori . Also, a priA null mutant was more sensitive to DNA‐damaging agents and was much more sensitive to acid and oxidative stress as compared to the wild‐type strain. Conclusions These data suggest that the PriA protein is needed for survival and persistence of H. pylori in mice stomach mucosa.